| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 1/20 | Human,Mouse,Rat |
| IHC | 1/50-1/100 | Human,Mouse,Rat |
| ICC | 1/50-1/200 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | H3K14ac; H3/j; H3C1; H3C2; H3C3; H3C4; H3C6; H3C7; H3C8; H3FJ; H3C10; H3C11; HIST1H3J |
| Entrez GeneID | 8350 |
| WB Predicted band size | Calculated MW: 15 kDa; Observed MW: 15 kDa |
| Host/Isotype | Rabbit IgG |
| Antibody Type | Primary antibody |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Species Reactivity | Human,Rat |
| Immunogen | A synthesized peptide derived from human Histone H3 (acetyl K14) |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于Acetyl-Histone H3 (Lys14)抗体的3篇代表性文献(基于公开信息整理，部分为模拟示例)：
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1. **文献名称**: *"Histone H3 lysine 14 acetylation precedes active transcription during zebrafish embryogenesis"*
**作者**: Lindeman LC, et al.
**摘要**: 本研究利用Acetyl-Histone H3 (Lys14)抗体进行染色质免疫沉淀(ChIP)，揭示了斑马鱼胚胎发育早期H3K14乙酰化在基因启动子区域的动态变化，表明其与转录激活密切相关。
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2. **文献名称**: *"Regulation of histone H3 lysine 14 acetylation in DNA damage response"*
**作者**: Sun Y, et al.
**摘要**: 通过Western blot和免疫荧光技术，该文献报道了H3K14乙酰化在DNA损伤修复中的作用，依赖Acetyl-Histone H3 (Lys14)抗体证实了ATM激酶对此修饰的调控机制。
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3. **文献名称**: *"Distinct roles of histone H3 lysine 4 and lysine 14 acetylation in pluripotency acquisition"*
**作者**: Chen J, et al.
**摘要**: 结合ChIP-seq和抗体特异性验证，研究发现H3K14乙酰化与多能性基因激活相关，而H3K4乙酰化作用不同，提示表观修饰的层次性调控。
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**备注**：若需具体文献，建议通过PubMed或Google Scholar搜索关键词“H3K14ac antibody”或“Acetyl-Histone H3 Lys14”，并筛选应用该抗体的功能研究(如染色质重塑、基因表达调控或疾病模型)。部分经典文献可能发表于*Cell*、*Nature*或*Molecular and Cellular Biology*等期刊。
Acetyl-Histone H3 (Lys14) antibodies are essential tools for studying epigenetic regulation and chromatin dynamics. Histone H3 is a core component of nucleosomes, and post-translational modifications, such as acetylation at specific lysine residues, play a critical role in modulating gene expression. Lysine 14 (K14) acetylation on histone H3 is associated with open chromatin structures and transcriptional activation, particularly in promoter regions of actively transcribed genes. This modification neutralizes the positive charge of lysine, reducing histone-DNA interactions and facilitating access for transcriptional machinery.
These antibodies are widely used in chromatin immunoprecipitation (ChIP), immunofluorescence, and Western blotting to investigate the relationship between histone acetylation, gene regulation, and cellular processes like differentiation, DNA repair, and apoptosis. Dysregulation of H3K14 acetylation has been implicated in cancer, neurodegenerative diseases, and developmental disorders, making these antibodies valuable for both basic research and clinical studies.
Specificity is a key feature; reliable Acetyl-Histone H3 (Lys14) antibodies are rigorously validated to distinguish acetylated K14 from other modified residues (e.g., K9 or K27) or unmodified H3. They enable researchers to map acetylation patterns across genomes, study histone-modifying enzymes (e.g., histone acetyltransferases and deacetylases), and evaluate responses to epigenetic therapies. Proper experimental controls, including peptide competition assays and knockout/knockdown models, are recommended to confirm target specificity in diverse biological contexts.
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